Gluten is a structural protein naturally found in certain cereal grains. The term gluten usually refers to the elastic network of a wheat grain's proteins, gliadin and glutenin primarily, that forms readily with the addition of water and often kneading in the case of bread dough. The types of grains that contain gluten include all species of wheat, and barley, rye, and some cultivars of oat; moreover, cross hybrids of any of these cereal grains also contain gluten, e.g. triticale. Gluten makes up 75–85% of the total protein in bread wheat.
Protein biosynthesis is a core biological process, occurring inside cells, balancing the loss of cellular proteins through the production of new proteins. Proteins perform a number of critical functions as enzymes, structural proteins or hormones. Protein synthesis is a very similar process for both prokaryotes and eukaryotes but there are some distinct differences.
Bread is a staple food prepared from a dough of flour and water, usually by baking. Throughout recorded history and around the world, it has been an important part of many cultures' diet. It is one of the oldest human-made foods, having been of significance since the dawn of agriculture, and plays an essential role in both religious rituals and secular culture.
Protein folding is the physical process by which a protein, after synthesis by a ribosome as a linear chain of amino acids, changes from an unstable random coil into a more ordered three-dimensional structure. This structure permits the protein to become biologically functional.
In chemistry, a disulfide is a compound containing a R−S−S−R′ functional group or the S2−
2 anion. The linkage is also called an SS-bond or sometimes a disulfide bridge and usually derived from two thiol groups.
A croissant is a French pastry made from puff pastry in a crescent shape.
Angel food cake, or angel cake, is a type of sponge cake made with egg whites, flour, and sugar. A whipping agent, such as cream of tartar, is commonly added. It differs from other cakes because it uses no butter. Its aerated texture comes from whipped egg white. Angel food cake originated in the United States and first became popular in the late 19th century. It gained its unique reputation along with its name due to its light and fluffy texture and white color.
Spelt, also known as dinkel wheat or hulled wheat, is a species of wheat that has been cultivated since approximately 5000 BCE.
Protein structure is the three-dimensional arrangement of atoms in an amino acid-chain molecule. Proteins are polymers – specifically polypeptides – formed from sequences of amino acids, which are the monomers of the polymer. A single amino acid monomer may also be called a residue, which indicates a repeating unit of a polymer. Proteins form by amino acids undergoing condensation reactions, in which the amino acids lose one water molecule per reaction in order to attach to one another with a peptide bond. By convention, a chain under 30 amino acids is often identified as a peptide, rather than a protein. To be able to perform their biological function, proteins fold into one or more specific spatial conformations driven by a number of non-covalent interactions, such as hydrogen bonding, ionic interactions, Van der Waals forces, and hydrophobic packing. To understand the functions of proteins at a molecular level, it is often necessary to determine their three-dimensional structure. This is the topic of the scientific field of structural biology, which employs techniques such as X-ray crystallography, NMR spectroscopy, cryo-electron microscopy (cryo-EM) and dual polarisation interferometry, to determine the structure of proteins.
Gliadin is a class of proteins present in wheat and several other cereals within the grass genus Triticum. Gliadins, which are a component of gluten, are essential for giving bread the ability to rise properly during baking. Gliadins and glutenins are the two main components of the gluten fraction of the wheat seed. This gluten is found in products such as wheat flour. Gluten is split about evenly between the gliadins and glutenins, although there are variations found in different sources.
Macroglobulins are large globular proteins and are found in the blood and other body fluids. Various physiological processes, including immunity, coagulation, and chemical transport, rely on these proteins. A macroglobulin is a plasma globulin of high molecular weight. Elevated levels of macroglobulins (macroglobulinemia) may cause manifestations of excess blood viscosity and/or precipitate within blood vessels when temperature drops. Other macroglobulins include α2-macroglobulin, which is elevated in nephrotic syndrome, diabetes, severe burns, and other conditions, while a deficiency is associated with chronic obstructive pulmonary disease.
Diphtheria toxin is an exotoxin secreted mainly by Corynebacterium diphtheriae but also by Corynebacterium ulcerans and Corynebacterium pseudotuberculosis, the pathogenic bacterium that causes diphtheria. The toxin gene is encoded by a prophage called corynephage β. The toxin causes the disease in humans by gaining entry into the cell cytoplasm and inhibiting protein synthesis.
Prolamins are a group of plant storage proteins having a high proline amino acid content. They are found in plants, mainly in the seeds of cereal grains such as wheat (gliadin), barley (hordein), rye (secalin), corn (zein), sorghum (kafirin), and oats (avenin). They are characterised by a high glutamine and proline content, and have poor solubility in water. They solubilise best in strong alcohol (70–80%), light acid, and alkaline solutions. The prolamins of the tribe Triticeae, such as wheat gliadin, and related proteins are known to trigger coeliac disease, an autoimmune condition, in genetically predisposed individuals.
Wheat allergy is an allergy to wheat which typically presents itself as a food allergy, but can also be a contact allergy resulting from occupational exposure. Like all allergies, wheat allergy involves immunoglobulin E and mast cell response. Typically the allergy is limited to the seed storage proteins of wheat. Some reactions are restricted to wheat proteins, while others can react across many varieties of seeds and other plant tissues. Wheat allergy is rare. Prevalence in adults was found to be 0.21% in a 2012 study in Japan.
Gluten is the seed storage protein in mature wheat seeds. It is the sticky substance in bread wheat which allows dough to rise and retain its shape during baking. The same, or very similar, proteins are also found in related grasses within the tribe Triticeae. Seed glutens of some non-Triticeae plants have similar properties, but none can perform on a par with those of the Triticeae taxa, particularly the Triticum species. What distinguishes bread wheat from these other grass seeds is the quantity of these proteins and the level of subcomponents, with bread wheat having the highest protein content and a complex mixture of proteins derived from three grass species.
Glutelins are a class of prolamin proteins found in the endosperm of certain seeds of the grass family. They constitute a major component of the protein composite collectively referred to as gluten. Glutenin is the most common glutelin, as it is found in wheat and is responsible for some of the refined baking properties in bread wheat. The glutelins of barley and rye have also been identified. Glutelins are the primary protein form of energy storage in the endosperm of rice grains.
The immunochemistry of Triticeae glutens is important in several inflammatory diseases. It can be subdivided into innate responses, class II mediated presentation, class I mediated stimulation of killer cells, and antibody recognition. The responses to gluten proteins and polypeptide regions differs according to the type of gluten sensitivity. The response is also dependent on the genetic makeup of the human leukocyte antigen genes. In gluten sensitive enteropathy, there are four types of recognition, innate immunity, HLA-DQ, and antibody recognition of gliadin and transglutaminase. With idiopathic gluten sensitivity only antibody recognition to gliadin has been resolved. In wheat allergy, the response pathways are mediated through IgE against other wheat proteins and other forms of gliadin.
Psathyrostachys juncea is a species of grass known by the common name Russian wildrye. It was formerly classified as Elymus junceus. It is native to Russia and China, and has been introduced to other parts of the world, such as Canada and the United States. Psathyrostachys juncea is a great source of food for grazing animals, as it has high nutrition value in its dense basal leaves, even in the late summer and autumn seasons. This species can grow and prosper in many harsh environments, making it an ideal candidate for improvement as it can grow in areas were farming is difficult. This species is a drought-resistant forage plant and can survive during the cool seasons. It is also a cross-pollinator and is self-sterile. This means that P. juncea cannot self-fertilize; it must find another plant of the same species with which to exchange gametes. Self-sterilization increases the genetic diversity of a species.
Caricain is an enzyme. This enzyme catalyses the following chemical reaction: Hydrolysis of proteins with broad specificity for peptide bonds, similar to those of papain and chymopapain
Cruciferin is one of the two most abundant seed storage proteins in mustard and rapeseed. They are classified as 11S globulins based on their sedimentation coefficient, and are salt soluble neutral glycoproteins. Their molecular weights range from 20 to 40 kDa. They comprise up to 50–70% of the total seed protein. Cruciferin is a comparatively larger seed storage protein than napin. It is composed of two polypeptide chains α and β. The α-chain has a mass of 30 kDa and the β-chain weighs in at 20 kDa. They are held together by a disulphide bond.
